Subcellular localization of vanillyl-alcohol oxidase in Penicillium simplicissimum.
Growth of Penicillium simplicissimum on anisyl alcohol, veratryl alcohol or 4-(methoxymethyl)phenol, is associated with the synthesis of relatively large amounts of the hydrogen peroxide producing flavoprotein vanillyl-alcohol oxidase (VAO). Immunocytochemistry revealed that the enzyme has a dual location namely in peroxisomes and in the cytosol. The C-terminus of the primary structure of VAO displays a WKL-COOH sequence which might function as a peroxisomal targeting signal type 1 (PTS1). As VAO activity results in production of hydrogen peroxide also the subcellular location of a recently characterized co-inducible catalase-peroxidase was studied. As VAO, this hydroperoxidase is also distributed throughout the cytosol and peroxisomes.
Fraaije
M W
MW
Department of Biomolecular Sciences, Laboratory of Biochemistry, Wageningen Agricultural University, The Netherlands.
Sjollema
K A
KA
Veenhuis
M
M
van Berkel
W J
WJ
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000438:Alcohols / Q000378:metabolism; D003600:Cytosol / Q000201:enzymology; D004790:Enzyme Induction / Q000235:genetics; D005420:Flavoproteins / Q000378:metabolism; D006861:Hydrogen Peroxide; D007150:Immunohistochemistry; D008830:Microbodies / Q000201:enzymology; D010407:Penicillium / Q000201:enzymology*; D010544:Peroxidases / Q000032:analysis; D021382:Protein Sorting Signals / Q000378:metabolism
D000438:Alcohols; D005420:Flavoproteins; D021382:Protein Sorting Signals; D006861:Hydrogen Peroxide; D000429:Alcohol Oxidoreductases; C076865:vanillyl-alcohol oxidase; D010544:Peroxidases